1gl8

SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORMSOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORM

Structural highlights 1gl8 is a 1 chain structure with sequence from Spiol. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1fb0, 1fb6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [TRXM_SPIOL] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Proton NMR spectral resonances of thioredoxin m from spinach have been assigned, and its solution structure has been determined on the basis of 1156 nuclear Overhauser effect- (NOE-) derived distance constraints by using restrained molecular dynamics calculations. The average pairwise root-mean-square deviation (RMSD) for the 25 best NMR structures for the backbone was 1.0 +/- 0.1, when the structurally well-defined residues were considered. The N- and C-terminal segments (1-13 and 118-119) and residues 41-49, comprising the active site, are highly disordered. At the time of concluding this work, a crystal structure of this protein was reported, in which thioredoxin m was found to crystallize as noncovalent dimers. Although the solution and crystal structures are very similar, no evidence was found about the existence of dimers in solution, thus confirming that dimerization is not needed for the regulatory activity of thioredoxin m. The spinach thioredoxin m does not unfold by heat in the range 25-85 degrees C, as revealed by thermal circular dichroic (CD) measurements. However, its unfolding free energy (9.1 +/- 0.8 kcal mol(-1), at pH 5.3 and 25 degrees C) could be determined by extrapolating the free energy values obtained at different concentrations of guanidinium chloride (GdmCl). The folding-unfolding process is two-state as indicated by the coincidence of the CD denaturation curves obtained at far and near UV. The H/D exchange behavior of backbone amide protons was analyzed. The slowest-exchanging protons, requiring a global-unfolding mechanism in order to exchange, are those from beta2, beta3, and beta4, the central strands of the beta-sheet, which constitute the main element of the core of the protein. The free energies obtained from exchange measurements of protons belonging to the alpha-helices are lower than those derived from GdmCl denaturation studies, indicating that those protons exchange by local-unfolding mechanisms. Three-dimensional solution structure and stability of thioredoxin m from spinach.,Neira JL, Gonzalez C, Toiron C, de Prat-Gay G, Rico M Biochemistry. 2001 Dec 18;40(50):15246-56. PMID:11735407 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioredoxin

spinqualitylabelsall models 1gl8, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image